ArticleProceedings of the National Academy of Sciences of the United States of America2024
Reassessing the exon-foldon correspondence using frustration analysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- From static structures to dynamic energy landscapes: the latest revolution in molecular biology.Current opinion in structural biology · 2026Review
- Predicting Protein Folding Dynamics Using Sequence Information.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Inferring protein-folding mechanisms from natural sequence diversity.Biophysical journal · 2025Article
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Reassessing the exon-foldon correspondence using frustration analysis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
5 authors.
Funding
Abstract
Protein folding and evolution are intimately linked phenomena. Here, we revisit the concept of exons as potential protein folding modules across a set of 38 abundant and conserved protein families. Taking advantage of genomic exon-intron organization and extensive protein sequence data, we explore exon boundary conservation and assess the foldon-like behavior of exons using energy landscape theoretic measurements. We found deviations in the exon size distribution from exponential decay indicating selection in evolution. We show that when taken together there is a pronounced tendency to independent foldability for segments corresponding to the more conserved exons, supporting the idea of exon-foldon correspondence. While 45% of the families follow this general trend when analyzed individually, there are some families for which other stronger functional determinants, such as preserving frustrated active sites, may be acting. We further develop a systematic partitioning of protein domains using exon boundary hotspots, showing that minimal common exons correspond with uninterrupted alpha and/or beta elements for the majority of the families but not for all of them.
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